2C4M
Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0008184 | molecular_function | glycogen phosphorylase activity |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0102250 | molecular_function | linear malto-oligosaccharide phosphorylase activity |
A | 0102499 | molecular_function | SHG alpha-glucan phosphorylase activity |
B | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0008184 | molecular_function | glycogen phosphorylase activity |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0102250 | molecular_function | linear malto-oligosaccharide phosphorylase activity |
B | 0102499 | molecular_function | SHG alpha-glucan phosphorylase activity |
C | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0008184 | molecular_function | glycogen phosphorylase activity |
C | 0016757 | molecular_function | glycosyltransferase activity |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0102250 | molecular_function | linear malto-oligosaccharide phosphorylase activity |
C | 0102499 | molecular_function | SHG alpha-glucan phosphorylase activity |
D | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0008184 | molecular_function | glycogen phosphorylase activity |
D | 0016757 | molecular_function | glycosyltransferase activity |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0102250 | molecular_function | linear malto-oligosaccharide phosphorylase activity |
D | 0102499 | molecular_function | SHG alpha-glucan phosphorylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A1794 |
Chain | Residue |
A | GLY113 |
A | GLY114 |
A | PLP1634 |
A | HOH2298 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 B1795 |
Chain | Residue |
B | SER174 |
B | HOH2088 |
B | HOH2300 |
A | THR28 |
A | ARG30 |
A | LYS31 |
B | ARG172 |
B | ALA173 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 B1796 |
Chain | Residue |
A | ARG172 |
A | ALA173 |
A | SER174 |
B | THR28 |
B | ARG30 |
B | LYS31 |
B | HOH2301 |
B | HOH2302 |
B | HOH2303 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 B1797 |
Chain | Residue |
A | ARG141 |
A | ARG234 |
A | GLU235 |
B | ARG141 |
B | ARG234 |
B | GLU235 |
B | HOH2129 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 B1798 |
Chain | Residue |
B | GLY113 |
B | GLY114 |
B | PLP1634 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 C1796 |
Chain | Residue |
C | THR28 |
C | ARG30 |
C | LYS31 |
C | HOH2019 |
C | HOH2337 |
D | ARG172 |
D | ALA173 |
D | SER174 |
D | HOH2064 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 C1797 |
Chain | Residue |
C | ARG141 |
C | ARG234 |
C | GLU235 |
C | HOH2091 |
C | HOH2145 |
C | HOH2338 |
D | ARG141 |
D | ARG234 |
D | GLU235 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 C1798 |
Chain | Residue |
C | GLY113 |
C | GLY114 |
C | ARG523 |
C | PLP1634 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 D1794 |
Chain | Residue |
C | ARG172 |
C | ALA173 |
C | SER174 |
C | HOH2107 |
D | THR28 |
D | ARG30 |
D | LYS31 |
D | HOH2202 |
D | HOH2203 |
site_id | BC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PLP A1634 |
Chain | Residue |
A | GLY114 |
A | TRP444 |
A | LYS522 |
A | ASN603 |
A | VAL604 |
A | THR630 |
A | SER631 |
A | LYS634 |
A | PO41794 |
A | HOH2056 |
A | HOH2247 |
site_id | BC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PLP B1634 |
Chain | Residue |
B | LEU69 |
B | GLY114 |
B | TRP444 |
B | LYS522 |
B | ASN603 |
B | VAL604 |
B | THR630 |
B | SER631 |
B | LYS634 |
B | PO41798 |
B | HOH2299 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B1801 |
Chain | Residue |
B | CYS180 |
B | TYR262 |
B | PHE353 |
B | ARG355 |
B | VAL356 |
B | HOH2304 |
B | HOH2305 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B1802 |
Chain | Residue |
B | TRP48 |
B | THR51 |
B | TYR55 |
B | THR134 |
B | VAL203 |
B | GLY204 |
B | THR205 |
B | HOH2306 |
site_id | BC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PLP C1634 |
Chain | Residue |
C | GLY114 |
C | TRP444 |
C | LYS522 |
C | ASN603 |
C | VAL604 |
C | THR630 |
C | SER631 |
C | LYS634 |
C | PO41798 |
C | HOH2244 |
C | HOH2336 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO C1803 |
Chain | Residue |
C | TRP48 |
C | THR51 |
C | TYR55 |
C | THR134 |
C | VAL203 |
C | GLY204 |
C | THR205 |
C | HOH2086 |
C | HOH2340 |
site_id | BC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PLP D1634 |
Chain | Residue |
D | GLY114 |
D | TRP444 |
D | ILE521 |
D | LYS522 |
D | ASN603 |
D | VAL604 |
D | GLY629 |
D | THR630 |
D | SER631 |
D | LYS634 |
D | HOH2148 |
D | HOH2201 |
site_id | BC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT A1795 |
Chain | Residue |
A | TYR136 |
A | MET272 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT A1796 |
Chain | Residue |
A | ARG52 |
A | ARG172 |
A | HOH2299 |
A | HOH2300 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT A1797 |
Chain | Residue |
A | CYS180 |
A | TYR262 |
A | PHE353 |
A | VAL356 |
A | HOH2301 |
A | HOH2302 |
site_id | CC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FMT A1798 |
Chain | Residue |
A | TRP48 |
A | TYR55 |
A | THR134 |
A | VAL203 |
A | GLY204 |
A | THR205 |
A | HOH2110 |
site_id | CC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT A1799 |
Chain | Residue |
A | GLY114 |
A | HIS334 |
A | ASN437 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A1800 |
Chain | Residue |
A | GLU659 |
A | GLU660 |
A | ALA662 |
A | TYR663 |
A | MET760 |
site_id | CC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT A1801 |
Chain | Residue |
A | HIS720 |
A | GLY721 |
D | HOH2186 |
site_id | CC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT A1802 |
Chain | Residue |
A | THR79 |
A | ASN80 |
A | TYR198 |
A | GLY199 |
site_id | CC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT A1803 |
Chain | Residue |
A | ARG355 |
A | HOH2303 |
site_id | CC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FMT B1799 |
Chain | Residue |
B | ARG355 |
site_id | CC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT B1800 |
Chain | Residue |
B | ASN80 |
B | TYR198 |
B | GLY199 |
site_id | DC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT C1799 |
Chain | Residue |
C | ASN80 |
C | GLY199 |
site_id | DC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT C1800 |
Chain | Residue |
C | CYS180 |
C | PHE353 |
C | ARG355 |
C | HOH2114 |
C | HOH2116 |
C | HOH2339 |
site_id | DC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT C1801 |
Chain | Residue |
C | THR79 |
C | ARG446 |
C | MET447 |
site_id | DC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT C1802 |
Chain | Residue |
C | ASP480 |
C | ASP481 |
C | LYS482 |
site_id | DC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT D1795 |
Chain | Residue |
D | TRP48 |
D | TYR55 |
D | VAL203 |
D | GLY204 |
D | THR205 |
D | HOH2049 |
site_id | DC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT D1796 |
Chain | Residue |
D | ALA66 |
D | ARG257 |
D | GLN261 |
D | HIS298 |
D | HOH2204 |
site_id | DC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT D1797 |
Chain | Residue |
D | TYR262 |
D | PHE353 |
D | ARG355 |
D | VAL356 |
D | HOH2205 |
site_id | DC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT D1798 |
Chain | Residue |
D | TRP318 |
D | ARG355 |
Functional Information from PROSITE/UniProt
site_id | PS00102 |
Number of Residues | 13 |
Details | PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtSnMKfmMN |
Chain | Residue | Details |
A | GLU626-ASN638 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1gpa |
Chain | Residue | Details |
A | LYS528 | |
A | ARG523 | |
A | LYS522 | |
A | THR630 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1gpa |
Chain | Residue | Details |
B | LYS528 | |
B | ARG523 | |
B | LYS522 | |
B | THR630 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1gpa |
Chain | Residue | Details |
C | LYS528 | |
C | ARG523 | |
C | LYS522 | |
C | THR630 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1gpa |
Chain | Residue | Details |
D | LYS528 | |
D | ARG523 | |
D | LYS522 | |
D | THR630 |